You Searched For: H-L-Dap(boc)-OMe·HCl


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Catalog Number: (BOSSBS-12980R-CY7)
Supplier: Bioss
Description: Protein kinase termed (DAPK2) dependant on calcium/calmodulin (Ca2+/CaM) contains an N-terminal protein kinase domain followed by a conserved CaM-binding domain with significant homologies to those of DAP kinase, a protein kinase involved in apoptosis. Overexpression of DAPK2 significantly induced the morphological changes characteristic of apoptosis. Results indicate that DAPK2 is an additional member of DAP kinase family involved in apoptotic signaling.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-3785R-CY3)
Supplier: Bioss
Description: Apoptosis is mediated by death domain containing adapter molecules and a caspase family of proteases. Certain serine/threonine protein kinases, such as ASK1 and RIP, are mediators of apoptosis. Two novel serine/threonine kinases that induce apoptosis were recently identified and designated DRAK1 and DRAK2 (for DAP kinase related apoptosis inducing protein kinases). DRAKs contain an N terminal kinase domain and a C terminal regulation domain. Overexpression of DRAK2 induces apoptosis. DRAKs have high sequence homology to DAP and ZIP kinases, and they represent a novel family of serine/threonine kinases, which mediates apoptosis through their catalytic activities. DRAK2 is located in nucleus and the messenger RNA was ubiquitously expressed in human tissues.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-3785R-CY5)
Supplier: Bioss
Description: Apoptosis is mediated by death domain containing adapter molecules and a caspase family of proteases. Certain serine/threonine protein kinases, such as ASK1 and RIP, are mediators of apoptosis. Two novel serine/threonine kinases that induce apoptosis were recently identified and designated DRAK1 and DRAK2 (for DAP kinase related apoptosis inducing protein kinases). DRAKs contain an N terminal kinase domain and a C terminal regulation domain. Overexpression of DRAK2 induces apoptosis. DRAKs have high sequence homology to DAP and ZIP kinases, and they represent a novel family of serine/threonine kinases, which mediates apoptosis through their catalytic activities. DRAK2 is located in nucleus and the messenger RNA was ubiquitously expressed in human tissues.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12980R-A647)
Supplier: Bioss
Description: Protein kinase termed (DAPK2) dependant on calcium/calmodulin (Ca2+/CaM) contains an N-terminal protein kinase domain followed by a conserved CaM-binding domain with significant homologies to those of DAP kinase, a protein kinase involved in apoptosis. Overexpression of DAPK2 significantly induced the morphological changes characteristic of apoptosis. Results indicate that DAPK2 is an additional member of DAP kinase family involved in apoptotic signaling.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12980R-A488)
Supplier: Bioss
Description: Protein kinase termed (DAPK2) dependant on calcium/calmodulin (Ca2+/CaM) contains an N-terminal protein kinase domain followed by a conserved CaM-binding domain with significant homologies to those of DAP kinase, a protein kinase involved in apoptosis. Overexpression of DAPK2 significantly induced the morphological changes characteristic of apoptosis. Results indicate that DAPK2 is an additional member of DAP kinase family involved in apoptotic signaling.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12138R-CY3)
Supplier: Bioss
Description: Members of the postsynaptic density-95 (PSD-95)/SAP90 family of membrane-associated guanylate kinase (MAGUK) proteins function as multimodular scaffolds that organize protein-signaling complexes at neuronal synapses. PSD-95/SAP90 binds guanylate kinase-associated protein (GKAP), also designated GK domain-binding protein, DAP-1-a, DAP-1-b, PSD-95 binding protein, PSD-95/SAP90 associated protein, or SAPAP, through the guanylate kinase domain. GKAP is expressed widely in neurons of the cortex and hippocampus and in the Purkinje and granule cells of the cerebellum. GKAP is localized specifically in the PSD of glutamatergic synapses, consistent with its direct interaction with PSD-95 family proteins.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12138R-CY5)
Supplier: Bioss
Description: Members of the postsynaptic density-95 (PSD-95)/SAP90 family of membrane-associated guanylate kinase (MAGUK) proteins function as multimodular scaffolds that organize protein-signaling complexes at neuronal synapses. PSD-95/SAP90 binds guanylate kinase-associated protein (GKAP), also designated GK domain-binding protein, DAP-1-a, DAP-1-b, PSD-95 binding protein, PSD-95/SAP90 associated protein, or SAPAP, through the guanylate kinase domain. GKAP is expressed widely in neurons of the cortex and hippocampus and in the Purkinje and granule cells of the cerebellum. GKAP is localized specifically in the PSD of glutamatergic synapses, consistent with its direct interaction with PSD-95 family proteins.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12138R-A488)
Supplier: Bioss
Description: Members of the postsynaptic density-95 (PSD-95)/SAP90 family of membrane-associated guanylate kinase (MAGUK) proteins function as multimodular scaffolds that organize protein-signaling complexes at neuronal synapses. PSD-95/SAP90 binds guanylate kinase-associated protein (GKAP), also designated GK domain-binding protein, DAP-1-a, DAP-1-b, PSD-95 binding protein, PSD-95/SAP90 associated protein, or SAPAP, through the guanylate kinase domain. GKAP is expressed widely in neurons of the cortex and hippocampus and in the Purkinje and granule cells of the cerebellum. GKAP is localized specifically in the PSD of glutamatergic synapses, consistent with its direct interaction with PSD-95 family proteins.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-1350R-A750)
Supplier: Bioss
Description: Death Associated Protein 5 (DAP5) is a 97 kDa protein with high amino acid sequence homology to Eukaryotic Translation Initiation Factor 4G (eIF4G). Compared with eIF4G, DAP5 lacks the N-terminal region necessary for cap-dependent translation and has a unique C-terminal part functioning as a regulator for interferon-gamma induced cell death. During apoptosis, DAP5 is cleaved at Asp790. The C-terminal truncated form of DAP5 functions as a cap-independent translation initiation factor responsible for the mediation of its own translation during apoptosis.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12138R-A680)
Supplier: Bioss
Description: Members of the postsynaptic density-95 (PSD-95)/SAP90 family of membrane-associated guanylate kinase (MAGUK) proteins function as multimodular scaffolds that organize protein-Signalling complexes at neuronal synapses. PSD-95/SAP90 binds guanylate kinase-associated protein (GKAP), also designated GK domain-binding protein, DAP-1-a, DAP-1-b, PSD-95 binding protein, PSD-95/SAP90 associated protein, or SAPAP, through the guanylate kinase domain. GKAP is expressed widely in neurons of the cortex and hippocampus and in the Purkinje and granule cells of the cerebellum. GKAP is localised specifically in the PSD of glutamatergic synapses, consistent with its direct interaction with PSD-95 family proteins.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-3785R-A750)
Supplier: Bioss
Description: Apoptosis is mediated by death domain containing adapter molecules and a caspase family of proteases. Certain serine/threonine protein kinases, such as ASK1 and RIP, are mediators of apoptosis. Two novel serine/threonine kinases that induce apoptosis were recently identified and designated DRAK1 and DRAK2 (for DAP kinase related apoptosis inducing protein kinases). DRAKs contain an N terminal kinase domain and a C terminal regulation domain. Overexpression of DRAK2 induces apoptosis. DRAKs have high sequence homology to DAP and ZIP kinases, and they represent a novel family of serine/threonine kinases, which mediates apoptosis through their catalytic activities. DRAK2 is located in nucleus and the messenger RNA was ubiquitously expressed in human tissues.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12138R-A647)
Supplier: Bioss
Description: Members of the postsynaptic density-95 (PSD-95)/SAP90 family of membrane-associated guanylate kinase (MAGUK) proteins function as multimodular scaffolds that organize protein-signaling complexes at neuronal synapses. PSD-95/SAP90 binds guanylate kinase-associated protein (GKAP), also designated GK domain-binding protein, DAP-1-a, DAP-1-b, PSD-95 binding protein, PSD-95/SAP90 associated protein, or SAPAP, through the guanylate kinase domain. GKAP is expressed widely in neurons of the cortex and hippocampus and in the Purkinje and granule cells of the cerebellum. GKAP is localized specifically in the PSD of glutamatergic synapses, consistent with its direct interaction with PSD-95 family proteins.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-3785R-CY7)
Supplier: Bioss
Description: Apoptosis is mediated by death domain containing adapter molecules and a caspase family of proteases. Certain serine/threonine protein kinases, such as ASK1 and RIP, are mediators of apoptosis. Two novel serine/threonine kinases that induce apoptosis were recently identified and designated DRAK1 and DRAK2 (for DAP kinase related apoptosis inducing protein kinases). DRAKs contain an N terminal kinase domain and a C terminal regulation domain. Overexpression of DRAK2 induces apoptosis. DRAKs have high sequence homology to DAP and ZIP kinases, and they represent a novel family of serine/threonine kinases, which mediates apoptosis through their catalytic activities. DRAK2 is located in nucleus and the messenger RNA was ubiquitously expressed in human tissues.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12138R-FITC)
Supplier: Bioss
Description: Members of the postsynaptic density-95 (PSD-95)/SAP90 family of membrane-associated guanylate kinase (MAGUK) proteins function as multimodular scaffolds that organize protein-signaling complexes at neuronal synapses. PSD-95/SAP90 binds guanylate kinase-associated protein (GKAP), also designated GK domain-binding protein, DAP-1-a, DAP-1-b, PSD-95 binding protein, PSD-95/SAP90 associated protein, or SAPAP, through the guanylate kinase domain. GKAP is expressed widely in neurons of the cortex and hippocampus and in the Purkinje and granule cells of the cerebellum. GKAP is localized specifically in the PSD of glutamatergic synapses, consistent with its direct interaction with PSD-95 family proteins.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12138R-A350)
Supplier: Bioss
Description: Members of the postsynaptic density-95 (PSD-95)/SAP90 family of membrane-associated guanylate kinase (MAGUK) proteins function as multimodular scaffolds that organize protein-signaling complexes at neuronal synapses. PSD-95/SAP90 binds guanylate kinase-associated protein (GKAP), also designated GK domain-binding protein, DAP-1-a, DAP-1-b, PSD-95 binding protein, PSD-95/SAP90 associated protein, or SAPAP, through the guanylate kinase domain. GKAP is expressed widely in neurons of the cortex and hippocampus and in the Purkinje and granule cells of the cerebellum. GKAP is localized specifically in the PSD of glutamatergic synapses, consistent with its direct interaction with PSD-95 family proteins.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12138R-HRP)
Supplier: Bioss
Description: Members of the postsynaptic density-95 (PSD-95)/SAP90 family of membrane-associated guanylate kinase (MAGUK) proteins function as multimodular scaffolds that organize protein-signaling complexes at neuronal synapses. PSD-95/SAP90 binds guanylate kinase-associated protein (GKAP), also designated GK domain-binding protein, DAP-1-a, DAP-1-b, PSD-95 binding protein, PSD-95/SAP90 associated protein, or SAPAP, through the guanylate kinase domain. GKAP is expressed widely in neurons of the cortex and hippocampus and in the Purkinje and granule cells of the cerebellum. GKAP is localized specifically in the PSD of glutamatergic synapses, consistent with its direct interaction with PSD-95 family proteins.
UOM: 1 * 100 µl


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Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the call is still displayed and you need assistance, please call us on +353 1 88 22222.
This product is marked as restricted and can only be purchased by approved Shipping Accounts. If you need further assistance, email VWR Regulatory Department at eurega_services@eu.vwr.com
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